4.5 Article

Alteration of N-glycan expression profile and glycan pattern of glycoproteins in human hepatoma cells after HCV infection

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1861, Issue 5, Pages 1036-1045

Publisher

ELSEVIER
DOI: 10.1016/j.bbagen.2017.02.014

Keywords

Glycosyltransferase expression analysis; Hepatitis C virus (HCV); Lectin microarray; Mass spectrometry; N-glycan; alpha 1,6-fucosyltransferase 8 (FUT8)

Funding

  1. National Natural Science Foundation of China [21572173, 31370197, 31221061]
  2. National Outstanding Youth Foundation of China [81025008]
  3. Hubei Province's Outstanding Medical Academic Leader Program [523276003]
  4. Hubei Province Major Knowledge Innovation Project (Natural Science Foundation) [2016CFA062, 2016ACA150]
  5. Grants-in-Aid for Scientific Research [15H04354] Funding Source: KAKEN

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Background: Hepatitis C virus (HCV) infection causes chronic liver diseases, liver fibrosis and even hepatocellular carcinoma (HCC). However little is known about any information of N-glycan pattern in human liver cell after HCV infection. Methods: The altered profiles of N-glycans in HCV-infected Huh7.5.1 cell were analyzed by using mass spectrometry. Then, lectin microarray, lectin pull-down assay, reverse transcription-quantitative real time PCR (RT-qPCR) and western-blotting were used to identify the altered N-glycosylated proteins and glycosyltransferases. Results: Compared to uninfected cells, significantly elevated levels of fucosylated, sialylated and complex N-glycans were found in HCV infected cells. Furthermore, Lens culinaris agglutinin (LCA)-binding glycoconjugates were increased most. Then, the LCA-agarose was used to precipitate the specific glycosylated proteins and identify that fucosylated modified annexin A2 (ANXA2) and heat shock protein 90 beta family member I (HSP90B1) was greatly increased in HCV-infected cells. However, the total ANXA2 and HSP90B1 protein levels remained unchanged. Additionally, we screened the mRNA expressions of 47 types of different glycosyltransferases and found that alpha 1,6-fucosyltransferase 8 (FUT8) was the most up-regulated and contributed to strengthen the LCA binding capability to fucosylated modified ANXA2 and HSP90B1 after HCV infection. Conclusions: HCV infection caused the altered N-glycans profiles, increased expressions of FUT8, fucosylated ANXA2 and HSP90B1 as well as enhanced LCA binding to Huh7.5.1. (C) 2017 Elsevier B.V. All rights reserved.

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